Conformational change in a viral glycoprotein during maturation due to disulfide bond disruption.
about
A single amino acid change in the Newcastle disease virus fusion protein alters the requirement for HN protein in fusionIntegrity of membrane lipid rafts is necessary for the ordered assembly and release of infectious Newcastle disease virus particlesNewcastle disease virus HN protein alters the conformation of the F protein at cell surfacesInhibition of receptor binding stabilizes Newcastle disease virus HN and F protein-containing complexes.The transmembrane domain sequence affects the structure and function of the Newcastle disease virus fusion protein.Thiol/disulfide exchange is required for membrane fusion directed by the Newcastle disease virus fusion protein.Mutational analysis of the leucine zipper motif in the Newcastle disease virus fusion protein.Postoligomerization folding of human cytomegalovirus glycoprotein B: identification of folding intermediates and importance of disulfide bonding.Incorporation of functional HN-F glycoprotein-containing complexes into newcastle disease virus is dependent on cholesterol and membrane lipid raft integrityNucleotide sequence and regulation of the Escherichia coli gene for ferrienterobactin transport protein FepB.Differential extractability of influenza virus hemagglutinin during intracellular transport in polarized epithelial cells and nonpolar fibroblasts.Mutations in the fusion peptide and heptad repeat regions of the Newcastle disease virus fusion protein block fusion.Complementation between avirulent Newcastle disease virus and a fusion protein gene expressed from a retrovirus vector: requirements for membrane fusionHomooligomerization of the hemagglutinin-neuraminidase glycoprotein of human parainfluenza virus type 3 occurs before the acquisition of correct intramolecular disulfide bonds and mature immunoreactivity.Intracellular processing of the paramyxovirus F protein: critical role of the predicted amphipathic alpha helix adjacent to the fusion domain.Addition of high-mannose sugars must precede disulfide bond formation for proper folding of Sendai virus glycoproteins.Strain variation and nuclear association of Newcastle disease virus matrix proteinAssignment of disulfide bridges in the fusion glycoprotein of Sendai virus.Mechanism of selective inhibition of respiratory syncytial virus by a benzodithiin compound (RD3-0028).Receptor-bound porcine epidemic diarrhea virus spike protein cleaved by trypsin induces membrane fusion.
P2860
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P2860
Conformational change in a viral glycoprotein during maturation due to disulfide bond disruption.
description
1987 nî lūn-bûn
@nan
1987 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
1987 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
1987年の論文
@ja
1987年論文
@yue
1987年論文
@zh-hant
1987年論文
@zh-hk
1987年論文
@zh-mo
1987年論文
@zh-tw
1987年论文
@wuu
name
Conformational change in a vir ...... to disulfide bond disruption.
@ast
Conformational change in a vir ...... to disulfide bond disruption.
@en
Conformational change in a vir ...... to disulfide bond disruption.
@nl
type
label
Conformational change in a vir ...... to disulfide bond disruption.
@ast
Conformational change in a vir ...... to disulfide bond disruption.
@en
Conformational change in a vir ...... to disulfide bond disruption.
@nl
prefLabel
Conformational change in a vir ...... to disulfide bond disruption.
@ast
Conformational change in a vir ...... to disulfide bond disruption.
@en
Conformational change in a vir ...... to disulfide bond disruption.
@nl
P2093
P2860
P356
P1476
Conformational change in a vir ...... to disulfide bond disruption.
@en
P2093
L W McGinnes
M E Peeples
T G Morrison
P2860
P304
P356
10.1073/PNAS.84.4.1020
P407
P577
1987-02-01T00:00:00Z